In terms of our years’ experience in single domain antibody realm, Creative Biolabs is able to assist our global clients in discovering and developing unique anti-albumin sdAbs with high specificity and affinity. Through our advanced phage display platform and comprehensive developability evaluations and selections, our scientists are confident in offering high-quality anti-albumin sdAbs exhibit efficient properties with high purity and yield.
Single domain antibody (sdAb), also known as domain antibody (dAb), is an antibody fragment generally derived from the novel heavy chain antibody (camelid) or IgNAR (cartilaginous fishes). A single domain antibody consists of the variable domain of heavy chain (VHH of heavy chain antibody, VNAR of IgNAR, or even VH/VL domain of conventional antibody) with a significantly smaller size than conventional antibodies. Compared with the traditional antibody, the CDR3 region of natural single domain antibody is longer, and the disulfide bond can form a larger antigen-binding loop with the adjacent CDR region, thereby increasing the binding area of the single domain antibody to the antigen. Not only that, single domain antibodies have better tissue permeability and lower immunogenicity due to its smaller size and extreme stability. Based on these advantages, single domain antibody has contributed to a series of fantastic applications in immunoassay, diagnostics, and therapeutics, especially as a potential component in drug discovery and development pipeline. With extensive experience in sdAb discovery and development field, scientists from Creative Biolabs are pleased to assist our clients to own their novel sdAb with high affinity and specificity to their interest targets, especially for the human serum albumin.
As one of the popular biomarkers in drug discovery, human serum albumin has widely distributed in the human body and has good stability and long half-life in serum. According to its properties, the human serum albumin plays important roles in the detection and diagnosis of diseases, such as diabetes, kidney disease, and cardiovascular disease. Meanwhile, the human serum albumin is also a well-validated fusion partner with other therapeutic agents. It can be coupled with drugs by fusion expression, covalent coupling, and non-covalent coupling to improve drug efficacy and half-life. The interaction mechanism between FcRn and albumin is of great significance to the pharmacokinetics and pharmacodynamics of albumin carrier drugs.
Scientists from Creative Biolabs can tailor our advanced platform to generate novel anti-albumin sdAbs to meet our clients’ specific project objectives. Fusion with an anti-albumin sdAb is a potential option to extend the serum half-life of therapeutic agents. The well-developed anti-albumin sdAb will recognize the albumin after properly administration and allow the fused biopharmaceutical agent to be carried around the body, and to take on similar PK parameters with the albumin as well.
After the discovery of specific anti-albumin sdAbs, our scientists can then offer a series of development services to further characterize and improve the application of anti-albumin sdAbs, which including but not limited to antibody affinity measurement, sdAb affinity maturation, immunogenicity assessment, manufacturability assessment, human or humanized sdAb production, and bispecific sdAb development.
Based on our state-of-the-art technology and expertise, Creative Biolabs are specialized in the discovery and production of anti-albumin single domain antibodies. Our scientists are pleased to offer customized service to meet our clients’ the most specific demands. If you are interested in developing the novel anti-albumin sdAbs, please do not hesitate to inquire us for more details.
Fig. 3 Integrative structural models of HSA-sdAb complexes. (Zhuolun Shen, 2021)
In this paper, scientists have developed a series of powerful and high-affinity single-domain antibodies against human serum albumin (anti-HSA sdAbs), which are used to fuse with small biological agents to extend the half-life. They characterized the thermal stability, binding kinetics, and cross-species reactivity of anti-HSA sdAbs, drew their epitope maps, and analyzed the tetramer HSA-sdAb complex structurally. Compared with the short-lived single-domain antibody, the half-life of anti-HSA sdAb was significantly prolonged by 771-fold by a quantitative proteomic parallel assay. Anti-HSA sdAb has unique and diverse pharmacokinetics, which is positively correlated with its albumin binding affinity under in vivo pH values.
An anti-albumin single-domain antibody is a specific type of monoclonal antibody specifically used to bind and target albumin. Compared with traditional intact antibodies, anti-albumin single-domain antibodies are usually smaller, simpler, and composed of a single immunoglobulin domain. They are usually prepared by genetic engineering and optimized to improve their specificity and affinity. This single-domain antibody has potential significance for the research, diagnosis, and treatment of albumin-related diseases.
Drug delivery: anti-albumin single-domain antibodies can be used in drug delivery systems to improve the blood circulation time and stability of drugs by combining albumin so as to enhance the efficacy of drugs.
Cancer treatment: albumin usually presents an increased concentration in tumor tissue, so anti-albumin single-domain antibodies can be used to deliver anticancer drugs directly to tumor cells to enhance therapeutic efficacy and reduce side effects.
Diagnostics: anti-albumin single-domain antibodies can be used to develop diagnostic kits to detect albumin levels in the blood to help diagnose and monitor certain diseases.
Biological imaging: the use of fluorescence-labeled anti-albumin single-domain antibodies in biological imaging studies can help to observe the dynamic distribution and transport of albumin in vivo, so as to gain an in-depth understanding of its role in physiological and pathological processes.
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